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Molecular and Cellular Biology, December 1999, p. 8660-8672, Vol. 19, No. 12
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Characterization of a Fission Yeast SUMO-1 Homologue, Pmt3p, Required for Multiple Nuclear Events, Including the Control of Telomere Length and Chromosome Segregation

Katsunori Tanaka,1,* Junko Nishide,1 Koei Okazaki,2 Hiroaki Kato,1 Osami Niwa,2 Tsuyoshi Nakagawa,3 Hideyuki Matsuda,1 Makoto Kawamukai,1 and Yota Murakami4

Department of Applied Bioscience and Biotechnology, Faculty of Life and Environmental Science,1 and Research Institute of Molecular Genetics,3 Shimane University, Matsue 690-8504, Kazusa DNA Research Institute, Kisarazu 292-0812,2 and Department of Viral Oncology, Institute for Virus Research, Kyoto University, Kyoto 606-0857,4 Japan

Received 18 June 1999/Returned for modification 2 August 1999/Accepted 10 September 1999

Unlike ubiquitin, the ubiquitin-like protein modifier SUMO-1 and its budding yeast homologue Smt3p have been shown to be more important for posttranslational protein modification than for protein degradation. Here we describe the identification of the SUMO-1 homologue of fission yeast, which we show to be required for a number of nuclear events including the control of telomere length and chromosome segregation. A disruption of the pmt3+ gene, the Schizosaccharomyces pombe homologue of SMT3, was not lethal, but mutant cells carrying the disrupted gene grew more slowly. The pmt3Delta cells showed various phenotypes such as aberrant mitosis, sensitivity to various reagents, and high-frequency loss of minichromosomes. Interestingly, we found that pmt3+ is required for telomere length maintenance. Loss of Pmt3p function caused a striking increase in telomere length. When Pmt3p synthesis was restored, the telomeres became gradually shorter. This is the first demonstration of involvement of one of the Smt3p/SUMO-1 family proteins in telomere length maintenance. Fusion of Pmt3p to green fluorescent protein (GFP) showed that Pmt3p was predominantly localized as intense spots in the nucleus. One of the spots was shown to correspond to the spindle pole body (SPB). During prometaphase- and metaphase, the bright GFP signals at the SPB disappeared. These observations suggest that Pmt3p is required for kinetochore and/or SPB functions involved in chromosome segregation. The multiple functions of Pmt3p described here suggest that several nuclear proteins are regulated by Pmt3p conjugation.

* Corresponding author. Mailing address: Department of Applied Bioscience and Biotechnology, Faculty of Life and Environmental Science, Shimane University, 1060 Nishikawatsu, Matsue 690-8504, Shimane, Japan. Phone: 81-852-32-6587. Fax: 81-852-32-6092. E-mail address: ktanaka{at}life.shimane-u.ac.jp.

Molecular and Cellular Biology, December 1999, p. 8660-8672, Vol. 19, No. 12
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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